ADP-ribosylating toxins have been studied as a key to prevention and treatment of diseases caused by the toxin-producing infectious microorganisms, and these toxins have provided unique pathological tools for the study of the physiological functions fo their target proteins. Recently, we have purified and crystallized a novel ADP-ribosylating toxin from Bacillus thuringiensis which is not homologous to other known ADP-ribosylating toxin. The crystals can be successfully flash-frozen using 30% PEG200 as a cryo-precipitant and 3.5 E resolution data set has been collected using our local laboratory X-ray source. We also obtained three heavy atom derivatives, thimerosal, trimethyl lead acetate, and K2IrCl6 which crystals diffract only to about 4 E resolution.